Human amygdala involvement in Alzheimer's disease revealed by stereological and dia-PASEF analysis.

BM88 antigen (BM88) antioxidant protein 2 (AOP2) calpactin II calpactin-1 heavy chain (CAL1H) centaurin-alpha-1 (CENTA1) endonexin II (ENX2) nuclear chloride ion channel 27 (NCC27)

Journal

Brain pathology (Zurich, Switzerland)
ISSN: 1750-3639
Titre abrégé: Brain Pathol
Pays: Switzerland
ID NLM: 9216781

Informations de publication

Date de publication:
09 2023
Historique:
received: 07 03 2023
accepted: 06 06 2023
medline: 31 8 2023
pubmed: 19 6 2023
entrez: 18 6 2023
Statut: ppublish

Résumé

Alzheimer's disease (AD) is characterized by the accumulation of pathological amyloid-β (Aβ) and Tau proteins. According to the prion-like hypothesis, both proteins can seed and disseminate through brain regions through neural connections and glial cells. The amygdaloid complex (AC) is involved early in the disease, and its widespread connections with other brain regions indicate that it is a hub for propagating pathology. To characterize changes in the AC as well as the involvement of neuronal and glial cells in AD, a combined stereological and proteomic analysis was performed in non-Alzheimer's disease and AD human samples. The synaptic alterations identified by proteomic data analysis could be related to the volume reduction observed in AD by the Cavalieri probe without neuronal loss. The pathological markers appeared in a gradient pattern with the medial region (cortical nucleus, Co) being more affected than lateral regions, suggesting the relevance of connections in the distribution of the pathology among different brain regions. Generalized astrogliosis was observed in every AC nucleus, likely related to deposits of pathological proteins. Astrocytes might mediate phagocytic microglial activation, whereas microglia might play a dual role since protective and toxic phenotypes have been described. These results highlight the potential participation of the amygdala in the disease spreading from/to olfactory areas, the temporal lobe and beyond. Proteomic data are available via ProteomeXchange with identifier PXD038322.

Identifiants

pubmed: 37331354
doi: 10.1111/bpa.13180
pmc: PMC10467039
doi:

Substances chimiques

tau Proteins 0
Amyloid beta-Peptides 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

e13180

Informations de copyright

© 2023 The Authors. Brain Pathology published by John Wiley & Sons Ltd on behalf of International Society of Neuropathology.

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Auteurs

Melania Gonzalez-Rodriguez (M)

Neuroplasticity and Neurodegeneration Laboratory, CRIB, Ciudad Real Medical School, University of Castilla-La Mancha, Ciudad Real, Spain.

Sandra Villar-Conde (S)

Neuroplasticity and Neurodegeneration Laboratory, CRIB, Ciudad Real Medical School, University of Castilla-La Mancha, Ciudad Real, Spain.

Veronica Astillero-Lopez (V)

Neuroplasticity and Neurodegeneration Laboratory, CRIB, Ciudad Real Medical School, University of Castilla-La Mancha, Ciudad Real, Spain.

Patricia Villanueva-Anguita (P)

Neuroplasticity and Neurodegeneration Laboratory, CRIB, Ciudad Real Medical School, University of Castilla-La Mancha, Ciudad Real, Spain.

Isabel Ubeda-Banon (I)

Neuroplasticity and Neurodegeneration Laboratory, CRIB, Ciudad Real Medical School, University of Castilla-La Mancha, Ciudad Real, Spain.

Alicia Flores-Cuadrado (A)

Neuroplasticity and Neurodegeneration Laboratory, CRIB, Ciudad Real Medical School, University of Castilla-La Mancha, Ciudad Real, Spain.

Alino Martinez-Marcos (A)

Neuroplasticity and Neurodegeneration Laboratory, CRIB, Ciudad Real Medical School, University of Castilla-La Mancha, Ciudad Real, Spain.

Daniel Saiz-Sanchez (D)

Neuroplasticity and Neurodegeneration Laboratory, CRIB, Ciudad Real Medical School, University of Castilla-La Mancha, Ciudad Real, Spain.

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Classifications MeSH